Difference between revisions of "Petit 2018 MiP2018"

Latest revision as of 09:37, 20 August 2018

Decreasing cytosolic translation is beneficial to yeast and human Tafazzin-deficient cells with dirupted mitochondrial homeostasis (Barth syndrome cell model).

Link: MiP2018

De Taffin de Tilques M, Lasserre JP, Godard F, Sardin E, Bouhier M, Le Guedard M, Kucharczyk R, Testet E, Di Rago JP, Tribouillard-Tanvier D, Petit PX (2018)

Event: MiP2018

Cardiolipin (CL) optimizes diverse mitochondrial processes, including oxidative phosphorylation (OXPHOS). To function properly, CL needs to be unsaturated, which requires the acyltransferase Tafazzin (TAZ)[1].

Loss-of-function mutations in the TAZ gene are responsible for the Barth syndrome (BTHS), a rare X-linked cardiomyopathy, presumably because of a diminished OXPHOS capacity [2]. Herein we show that a partial inhibition of cytosolic protein synthesis, either chemically with the use of cycloheximide or by specific genetic mutations, fully restores biogenesis and the activity of the oxidative phosphorylation system in a yeast BTHS model (taz1Δ). Interestingly, the defaults in CL were not suppressed, indicating that they are not primarily responsible for the OXPHOS deficiency in taz1Δ yeast.

Low concentrations of cycloheximide in the picomolar range were beneficial to TAZ-deficient HeLa cells, as evidenced by the recovery of a good proliferative capacity. These findings reveal that a diminished capacity of CL remodeling deficient cells to preserve protein homeostasis is likely an important factor contributing to the pathogenesis of BTHS. This in turn, identifies cytosolic translation as a potential therapeutic target for the treatment of this disease[3].

• Bioblast editor: Plangger M, Kandolf G

Labels: MiParea: mt-Biogenesis;mt-density, nDNA;cell genetics Pathology: Myopathy

Organism: Human, Saccharomyces cerevisiae Tissue;cell: HeLa

Affiliations

De Taffin de Tilques M(2), Lasserre JP(2), Godard F, Sardin E, Bouhier M, Le Guedard M, Kucharczyk R, Testet E, Di Rago JP(2), Tribouillard-Tanvier D(2), Petit PX(1)

CNRS FR3636, Inst de Neurosciences, Univ Paris-Descartes
Inst de Biochimie et génétique cellulaire, CNRS UMR 5095, Univ de Bordeaux; France. - [email protected]

References

Saric A, Andreau K, Armand AS, Møller IM, Petit PX (2016) Barth Syndrome: from mitochondrial dysfunctions associated with aberrant production of reactive oxygen species to pluripotent stem cell studies. Front Genet 6:359.
Gonzalvez F, D'Aurelio M, Boutant M, Moustapha A, Puech JP, Landes T, Arnauné-Pelloquin L, Vial G, Taleux N, Slomianny C, Wanders RJ, Houtkooper RH, Bellenguer P, Møller IM, Gottlieb E, Vaz FM, Manfredi G, Petit PX (2013) Barth syndrome: cellular compensation of mitochondrial dysfunction and apoptosis inhibition due to changes in cardiolipin remodeling linked to tafazzin (TAZ) gene mutation. Biochim Biophys Acta 1832:1194-206.
de Taffin de Tilques M, Lasserre JP, Godard F, Sardin E, Bouhier M, Le Guedard M, Kucharczyk R, Petit PX, Testet E, di Rago JP, Tribouillard-Tanvier D (2018) Decreasing cytosolic translation is beneficial to yeast and human Tafazzin-deficient cells. Microb Cell 5:220–32.

@@ Line 1: / Line 1: @@
 {{Abstract
-|title=[[Image:MiPsocietyLOGO.JPG|left|90px|Mitochondrial Physiology Society|MiPsociety]] Decreasing cytosolic translation is beneficial to yeast and human Tafazzin-deficient cells with dirupted mitochondrial homeostasis (Barth syndrome cell model).
+|title=[[Image:PetitP.jpg|left|90px|Patrice Petit]] Decreasing cytosolic translation is beneficial to yeast and human Tafazzin-deficient cells with dirupted mitochondrial homeostasis (Barth syndrome cell model).
 |info=[[MiP2018]]
-|authors=M. de Taffin de Tilques, J.-P. Lasserre, F. Godard, E. Sardin, M. Bouhier, M. Le Guedard, R. Kucharczyk, E. Testet, J.-P. di Rago, D. Tribouillard-Tanvier and P.X. Petit
+|authors=De Taffin de Tilques M, Lasserre JP, Godard F, Sardin E, Bouhier M, Le Guedard M, Kucharczyk R, Testet E, Di Rago JP, Tribouillard-Tanvier D, Petit PX
 |year=2018
 |event=MiP2018
-|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action MITOEAGLE]]
+|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action MitoEAGLE]]
-Cardiolipin (CL) optimizes diverse mitochondrial processes, includ-ing oxidative phosphorylation (OXPHOS). To function properly, CL needs to be unsaturated, which requires the acyltransferase Tafazzin (TAZ) [1].
+Cardiolipin (CL) optimizes diverse mitochondrial processes, including oxidative phosphorylation (OXPHOS). To function properly, CL needs to be unsaturated, which requires the acyltransferase Tafazzin (TAZ)[1].
-	Loss-of-function mutations in the TAZ gene are responsible for the Barth syndrome (BTHS), a rare X-linked cardiomyopathy, presumably because of a diminished OXPHOS capacity [2]. Herein we show that a partial inhibition of cytosolic protein synthesis, either chemically with the use of cycloheximide or by specific genetic mutations, fully restores biogenesis and the activity of the oxidative phosphorylation system in a yeast BTHS model (taz1Δ). Interestingly, the defaults in CL were not suppressed, indicating that they are not primarily responsible for the OXPHOS deficiency in taz1Δ yeast.
-	Low concentrations of cycloheximide in the picomolar range were beneficial to TAZ-deficient HeLa cells, as evidenced by the recovery of a good proliferative capacity. These findings reveal that a diminished capacity of CL remodeling deficient cells to preserve protein homeostasis is likely an important factor contributing to the pathogenesis of BTHS. This in turn, identifies cytosolic translation as a potential therapeutic target for the treatment of this disease [3]
+Loss-of-function mutations in the TAZ gene are responsible for the Barth syndrome (BTHS), a rare X-linked cardiomyopathy, presumably because of a diminished OXPHOS capacity [2]. Herein we show that a partial inhibition of cytosolic protein synthesis, either chemically with the use of cycloheximide or by specific genetic mutations, fully restores biogenesis and the activity of the oxidative phosphorylation system in a yeast BTHS model (''taz''1Δ). Interestingly, the defaults in CL were not suppressed, indicating that they are not primarily responsible for the OXPHOS deficiency in ''taz''1Δ yeast.
+Low concentrations of cycloheximide in the picomolar range were beneficial to TAZ-deficient HeLa cells, as evidenced by the recovery of a good proliferative capacity. These findings reveal that a diminished capacity of CL remodeling deficient cells to preserve protein homeostasis is likely an important factor contributing to the pathogenesis of BTHS. This in turn, identifies cytosolic translation as a potential therapeutic target for the treatment of this disease[3].
 |editor=[[Plangger M]], [[Kandolf G]],
 }}
 {{Labeling
-|area=nDNA;cell genetics
+|area=mt-Biogenesis;mt-density, nDNA;cell genetics
 |diseases=Myopathy
 |organism=Human, Saccharomyces cerevisiae
@@ Line 18: / Line 20: @@
 }}
 == Affiliations ==
-M. de Taffin de Tilques(2), J.-P. Lasserre(2), F. Godard, E. Sardin, M. Bouhier, M. Le Guedard, R. Kucharczyk, E. Testet, J.-P. di Rago(2), D. Tribouillard-Tanvier(2) and P.X. Petit(1)
+De Taffin de Tilques M(2), Lasserre JP(2), Godard F, Sardin E, Bouhier M, Le Guedard M, Kucharczyk R, Testet E, Di Rago JP(2), Tribouillard-Tanvier D(2), Petit PX(1)
-::::#CNRS FR3636, Institut de Neurosciences, Univ Paris-Descartes, France
+::::#CNRS FR3636, Inst de Neurosciences, Univ Paris-Descartes
-::::#Inst de Biochimie et génétique cellulaire, CNRS UMR 5095, Univ de Bordeaux, France.
+::::#Inst de Biochimie et génétique cellulaire, CNRS UMR 5095, Univ de Bordeaux; France. - [email protected]
 == References ==
-#Saric A, … Petit PX. Front Genet. 2016 Jan 20;6:359.
+::::#Saric A, Andreau K, Armand AS, Møller IM, Petit PX (2016) Barth Syndrome: from mitochondrial dysfunctions associated with aberrant production of reactive oxygen species to pluripotent stem cell studies. Front Genet 6:359.
-#Gonzalvez F, … Petit PX. Biochim Biophys Acta. 2013 Aug; 1832 (8): 1194-206.
+::::#Gonzalvez F, D'Aurelio M, Boutant M, Moustapha A, Puech JP, Landes T, Arnauné-Pelloquin L, Vial G, Taleux N, Slomianny C, Wanders RJ, Houtkooper RH, Bellenguer P, Møller IM, Gottlieb E, Vaz FM, Manfredi G, Petit PX (2013) Barth syndrome: cellular compensation of mitochondrial dysfunction and apoptosis inhibition due to changes in cardiolipin remodeling linked to tafazzin (TAZ) gene mutation. Biochim Biophys Acta 1832:1194-206.
-#de Taffin de Tilques M, … Tribouillard-Tanvier D. Microb Cell. 2018 Feb 18;5(5):220-232.
+::::#de Taffin de Tilques M, Lasserre JP, Godard F, Sardin E, Bouhier M, Le Guedard M, Kucharczyk R, Petit PX, Testet E, di Rago JP, Tribouillard-Tanvier D (2018) Decreasing cytosolic translation is beneficial to yeast and human Tafazzin-deficient cells. Microb Cell 5:220–32.